D8043
Anti-Dystrophin Antibody
mouse monoclonal, MANDRA1
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Product Name
Monoclonal Anti-Dystrophin antibody produced in mouse, clone MANDRA1, ascites fluid
biological source
mouse
conjugate
unconjugated
antibody form
ascites fluid
antibody product type
primary antibodies
clone
MANDRA1, monoclonal
contains
15 mM sodium azide
species reactivity
rat, human, mouse, fish
technique(s)
indirect immunofluorescence: 1:100 using freshly dissected and frozen human or animal muscle tissue.
microarray: suitable
isotype
IgG1
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Quality Level
Gene Information
human ... DMD(1756)
mouse ... Dmd(13405)
rat ... Dmd(24907)
1 of 4
This Item | D8168 | SAB4200763 | ZMS1051 |
|---|---|---|---|
| clone MANDRA1, monoclonal | clone MANDYS8, monoclonal | clone MANDRA1, monoclonal | clone C26, recombinant monoclonal |
| antibody form ascites fluid | antibody form ascites fluid | antibody form purified from hybridoma cell culture | antibody form purified antibody |
| Gene Information human ... DMD(1756) | Gene Information human ... DMD(1756) | Gene Information human ... DMD(1756) | Gene Information - |
| conjugate unconjugated | conjugate unconjugated | conjugate - | conjugate unconjugated |
| species reactivity rat, human, mouse, fish | species reactivity chicken, rat, human, pig, rabbit, mouse | species reactivity zebrafish, rat, mouse, human | species reactivity human |
| biological source mouse | biological source mouse | biological source mouse | biological source mouse |
Application
Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Immunofluorescence (1 paper)
Western Blotting (1 paper)
Immunofluorescence (1 paper)
Western Blotting (1 paper)
Mouse monoclonal clone MANDRA1 anti-Dystrophin antibody may be used for the localization of dystrophin using various immunochemical assays such as ELISA, capture ELISA, immunoblot, and immunohistochemistry. Monoclonal antibodies against defined regions of dystrophin provide a means for studying its structure and function, interactions with other proteins and the nature of the partial gene products produced in some patients carrying deletions in the dystrophin gene. The antibodies are useful in the prenatal or post-abortion diagnosis of muscular dystrophy carriers by immunohistological analyses.
Biochem/physiol Actions
The antibody recognizes an epitope located on the 128 amino acids at the end of the C-terminal domain of the human dystrophin molecule (amino acid residues 3558-3684). Immunohistochemical staining of muscle tissue results in a clear labeling confined to the periphery (plasma membrane) of normal striated muscle fibers. By immunoblotting, the antibody stains dystrophin (427 kDa) in muscle and brain extracts. It also stains the 70-75 kDa protein known as Apo-Dystrophin-1 or Dp71.4 This is detected in the brain as well as in lymphoblastoid cells, cultures of brain astroglial and neuronal cells, liver and Hep G2 cells (human hepatoma). The epitope recognized by the antibody is sensitive to formalin fixation and paraffin embedding. The antibody exhibits a wide interspecies cross-reactivity. It is useful in ELISA and capture ELISA. The antibody is specific to dystrophin and does not react with α-actinin and utrophin, an autosomal homologue of dystrophin, also called dystrophin-related protein (DRP).
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
General description
Dystrophin is a muscle membrane protein (427 kDa) which is absent, reduced or altered as a result of mutation in Duchenne and Becker muscular dystrophies (DMD/BMD) or its homologue in the mouse. Severe DMD is associated with a marked dystrophin deficiency whereas patients with the milder form of DMD show less pronounced abnormalities of protein expression. Because abnormalities in the protein expression occur specifically in patients with these types of muscular dystrophy, dystrophin analysis may be used to distinguish these conditions from other neuromuscular diseases. Predictions from the sequence suggest a structural protein on the inner face of the membrane, consisting of a 25-repeat, rod-like triple-helical domain separating an N-terminal actin-binding domain from two C-terminal domains, one of which is rich in cysteine. The large size of dystrophin and its low abundance (<0.01% of the total muscle protein) are a hindrance to the isolation of intact, native protein for structure/function studies.
The C-terminal domain of the human dystrophin molecule (amino acids residues 3558-3684) is present in normal muscle tissue. It is also present in nearly all Becker muscular dystrophies, but is absent in cases of Duchenne muscular dystrophies and in the dystrophic mouse (mdx).
The antibody recognizes an epitope located on the 128 amino acids at the end of the C-terminal domain of the human dystrophin molecule (amino acid residues 3558-3684). Immunohistochemical staining of muscle tissue results in a clear labeling confined to the periphery (plasma membrane) of normal striated muscle fibers. By immunoblotting, the antibody stains dystrophin (427 kDa) in muscle and brain extracts. It also stains the 70-75 kDa protein known as Apo-Dystrophin-1 or Dp71.4 This is detected in the brain as well as in lymphoblastoid cells, cultures of brain astroglial and neuronal cells, liver and Hep G2 cells (human hepatoma). The epitope recognized by the antibody is sensitive to formalin fixation and paraffin embedding. The antibody exhibits a wide interspecies cross-reactivity. It is useful in ELISA and capture ELISA. The antibody is specific to dystrophin and does not react with α-actinin and utrophin, an autosomal homologue of dystrophin, also called dystrophin-related protein (DRP).
Immunogen
fusion protein containing the C-terminal amino acids of human dystrophine.
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Storage Class
13 - Non Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
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Julia Saifetiarova et al.
Journal of neuroscience research, 95(7), 1373-1390 (2017-04-04)
Bidirectional interactions between neurons and myelinating glial cells result in formation of axonal domains along myelinated fibers. Loss of axonal domains leads to detrimental consequences on nerve structure and function, resulting in reduced conductive properties and the diminished ability to
Kazumi Zushi et al.
Journal of the Japanese Physical Therapy Association = Rigaku ryoho, 15(1), 1-8 (2012-01-01)
The purpose of this study was to investigate the effect of reloading on atrophied muscle and the time course of hypertrophy and regeneration. Forty-nine male Wistar rats were randomly assigned to groups for hindlimb suspension (HS), hindlimb suspension and reloading
G E Morris et al.
Journal of immunological methods, 161(1), 23-28 (1993-05-05)
A novel approach to the quantitation of the muscular dystrophy protein, dystrophin, in muscle extracts is described. The two-site ELISA uses two monoclonal antibodies against dystrophin epitopes which lie close together in the rod domain of the dystrophin molecule in
Beatrice Nico et al.
Laboratory investigation; a journal of technical methods and pathology, 90(11), 1645-1660 (2010-08-18)
In this study, we investigated the involvement of dystrophin-associated proteins (DAPs) and their relationship with the perivascular basement membrane in the brains of mdx mice and controls at the age of 2 months. We analyzed (1) the expression of glial
Meiling Zhang et al.
PloS one, 10(7), e0132567-e0132567 (2015-07-18)
Mitochondrial flash (mitoflash) is a highly-conserved, universal, and physiological mitochondrial activity in isolated mitochondria, intact cells, and live organisms. Here we investigated developmental and disease-related remodeling of mitoflash activity in zebrafish skeletal muscles. In transgenic zebrafish expressing the mitoflash reporter
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